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. 2022 Mar 16;18(3):e1009178. doi: 10.1371/journal.pcbi.1009178

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© 2022 Scheck et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 3 — A) Sequence recovery benchmark pipeline. Sequences in the interfaces of protein-protein complexes are evaluated in the presence and absence of the binding partner. The tested complexes were grouped into interfaces with low and high shape complementarity, and antibody-antigen complexes. Surface-centric design (RosettaSurf and RosettaSurf-site) is compared to a standard structural protein design protocol (FixBB). B) Interface sequence recovery of the complete dataset. C) Sequence recovery of low shape complementarity interfaces. D) Sequence recovery of high shape complementarity interfaces. E) Sequence recovery of antigen-antibody complexes. Dashed lines represent median and triangles represent mean recovery values.